Abstract
We have examined the band 3 protein(s) of rabbit erythrocyte membranes by a combination of differential extraction and surface labeling methods. Only one major peptide was labeled when intact red cells were exposed to 125I − and lactoperoxidase; this coincided with band 3. When intact cells were exposed to galactose oxidase followed by [ 3H]borohydride, numerous surface glycoproteins were labeled, one of which clearly coincided with band 3. Differential extraction with lithium diiodosalicylate revealed one major band 3 glycoprotein which contained both the 125I − and 3H surface labels and three peptides which were unlabeled; these three peptides are apparently not exposed at the cell surface.
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